capillary zone electrophoresis
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Talanta ◽  
2022 ◽  
Vol 237 ◽  
pp. 122945
Author(s):  
Maria Patrícia do Nascimento ◽  
Rafael Marques ◽  
Mathias Prado Pereira ◽  
Rafaela de Souza Martins ◽  
Fernanda Irene Bombonato ◽  
...  

Author(s):  
Rachel D Wheeler ◽  
Micsha V Costa ◽  
Asante Crichlow ◽  
Fenella Willis ◽  
Yasmin Reyal ◽  
...  

Multiple myeloma is a haematological cancer caused by malignant plasma cells in the bone marrow that can result in organ dysfunction and death. Recent novel treatments have contributed to improved survival rates, including monoclonal antibody therapies that target the CD38 protein on the surface of plasma cells. Anti-CD38 therapies are IgG kappa monoclonal antibodies that are given in doses high enough for the drug to be visible on serum protein electrophoresis as a small paraprotein. We present a case where isatuximab, the most recent anti-CD38 monoclonal antibody to be approved for treatment of myeloma, obscured the patient’s paraprotein on gel immunofixation, so that complete remission could not be demonstrated. This was resolved using the isatuximab Hydrashift assay. The interference on gel immunofixation was unexpected because isatuximab migrated in a position distinct from the patient’s paraprotein on capillary zone electrophoresis. We demonstrate the surprising finding that isatuximab migrates in a different position on gel electrophoresis compared to capillary zone electrophoresis. It is vital that laboratories are aware of the possible interference on electrophoresis from anti-CD38 monoclonal antibody therapies, and are able to recognise these drugs on protein electrophoresis. The difference in isatuximab’s electrophoretic mobility on capillary and gel protein electrophoresis makes this particularly challenging. Laboratories should have a strategy for alternative analyses in the event that the drugs interfere with assessment of the patient’s paraprotein.


2021 ◽  
Vol 79 (6) ◽  
pp. 567-578
Author(s):  
Alexandre Lasse ◽  
Marc Deveaux ◽  
Jean-Louis Beaudeux ◽  
Jean-Herlé Raphalen ◽  
Frédéric J Baud ◽  
...  

2021 ◽  
Vol 15 (11) ◽  
pp. 2893-2896
Author(s):  
Nada Sikander ◽  
Shabnam Bashir ◽  
Rija Tariq ◽  
Furqan Sabir ◽  
Samia Akhtar ◽  
...  

Background: Hemoglobin D Iran is frequently misdiagnosed as Hb E or Hb D Punjab if only one method of screening is used. The objective of our study was to highlight the importance of using two different screening techniques in diagnosis of a hemoglobin variant, Hb D Iran in our case. Hematological parameters of heterozygous Hb D Iran and compound heterozygous β/Hb D Iran were also compared. Methods: A descriptive study was carried out on results of 52,379 subjects which were part of thalassemia extended family cascade screening from 36 districts of Punjab from October 2019-March 2021. Cases of Hb D Punjab and Hb E were run on both CE-HPLC (cation exchange-high performance liquid chromatography) and CZE (capillary zone electrophoresis). Resulting Hb D Iran cases were confirmed by ARMS-PCR (Amplification refractory mutation system-polymerase chain reaction). Results: Forty cases of Hb D Iran were detected out of 160 initially suspected Hb D Punjab cases and 126 Hb E cases. Diagnosis was confirmed by molecular analysis. Statistical significance was found between RBC count, MCV, MCH, Hb F and diagnosis of “heterozygous Hb D Iran” and “compound heterozygous for β/ Hb D Iran”. Conclusion: Hb D Iran can be easily missed and misdiagnosed as Hb E or Hb D Punjab, if two screening methods are not used. This maybe a reason why Hb D Iran remains unreported in our region. CBC and HPLC indices can also be suggestive if a case is of heterozygous D Iran or compound heterozygous β/Hb D Iran. Keywords: Hb D Iran, Hb E, Hb D Punjab, Cation exchange High performance liquid chromatography, Capillary zone electrophoresis


Abstract This study establishes a method for rapid detection of clonidine and cyproheptadine in foods of animal origin. In order to obtain the best detection method, capillary zone electrophoresis (CZE), large volume sample stacking (LVSS), and sweeping-micellar electrokinetic capillary chromatography (sweeping-MEKC) were used respectively. The limits of detection (LODs) of clonidine and cyproheptadine by LVSS-CZE were 0.028 μg mL−1 and 0.034 μg mL−1, and those by sweeping-MEKC were 0.023 μg mL−1 and 0.031 μg mL−1, respectively. Compared with the CZE method, the two online pre-concentration technologies have greatly improved the detection sensitivity and achieved good enrichment results. However, compared with the sweeping-MEKC system, the LVSS system consumed a longer time and was greatly affected by the actual sample matrix. The sweeping-MEKC method was proved to be suitable for real sample analysis. Under the best sweeping-MEKC conditions, clonidine and cyproheptadine could be well separated within 8 min and good linear relationships in the range of 0.1–1.0 μg mL−1 (r 2 > 0.99) were obtained. This method was successfully applied to the determination of clonidine and cyproheptadine in animal-derived foods with the recoveries of 82.3%–90.1% and the relative standard deviations (RSDs) less than 3.11%. The sweeping-MEKC method is simple to operate and has great potential in the rapid detection of clonidine and cyproheptadine in animal-derived foods.


Blood ◽  
2021 ◽  
Vol 138 (Supplement 1) ◽  
pp. 2025-2025
Author(s):  
Susanna A Curtis ◽  
Elana M Friedman ◽  
Caterina Minniti ◽  
Annie Ngyuen Dang ◽  
Mira Pochron ◽  
...  

Abstract Background: Voxelotor (Oxbryta®) is a small molecule that binds to the alpha chain of hemoglobin (Hb) and increases the affinity of Hb for oxygen which reduces sickle Hb polymerization. It was approved by the FDA in 2019 for the treatment of sickle cell disease (SCD). Currently, the only method available to estimate the concentration of voxelotor in the blood is to obtain exposure measurements which are only available in select research laboratories. A method to measure voxelotor at a standard laboratory would allow clinicians to assess compliance and may be useful in determining optimal dosing. Case studies have reported that voxelotor binding to Hb interferes with capillary zone electrophoresis (CZE). As previously reported, in CZE the characteristic peaks of hemoglobin A2 (HbA2) and hemoglobin F (HbF) split in the presence of voxelotor. Interestingly, it does not cause the hemoglobin S peak to split. We posited that we could use this split to estimate the presence of voxelotor and whole blood concentration. Biophysical measurements of voxelotor binding to Hb were also measured in these samples. Methods: Patients were enrolled prospectively in an IRB approved protocol. Voxelotor was initiated at 1500 mg daily on day 0 and samples were taken at day 0 (pre-dose), 14, 30, and 60. Samples had Hb variants quantified by CZE using the Capillarys 2 FlexPiercing Instrument (Sebia, Georgia). Hematology parameters were measured with the Sysmex XN-1000 automated analyzer (Sysmex, Illinois). To determine whole blood concentration of voxelotor, samples were sent to Worldwide Clinical Trials where a validated liquid chromatography-tandem mass spectrometry method was used. Voxelotor's interference with HbA2 on CZE is dependent on the HbF percentage, therefore samples from patients with SCD were combined into three pooled samples (5-10 samples per pool) of HbF percentages spanning 5-30%. Three hundred µL aliquots of each pool were spiked with voxelotor in DMSO in triplicate to different concentrations between 0 and 600 µMol/L and were incubated at room temperature for 1 hour before being tested with CZE. Samples were then analyzed for voxelotor interference resulting in split peaks of HbF and HbA2. HbA2 interference percent (%VarA2) was calculated as the reported value of the HbA2 split peak over the total HbA2 value (both split and parent peak) times 100. F% was used as directly reported by the instrument without consideration of voxelotor interference. Results were then analyzed in Excel (Data Analytics package) using a multiparameter regression to generate a line of best fit. To allow for logarithmic fit when examining the correlation of calculated concentration with increase in Hb due to voxelotor, samples with negative Hb rises were excluded and concentrations which resulted as negative values were changed to 0.01 µM. Results: Of 20 patients which have been enrolled to date, 9 patients have completed the study and their data was used for these analyses. Using the CZE method described above the concentration of voxelotor was quantifiable using the following equation. Equation 1: uM voxelotor = -99.13 + 7.10*%HbF +12.52*%VarA2 The calculated concentrations of voxelotor based on CZE results had a strong correlation with whole blood concentration (R 2 = 0.85, p <0.001). (Figure 1) When calculated concentration was compared to change in Hb at days 14, 30, and 60 there was a significant positive logarithmic correlation between concentration and change in Hb (R 2=.56, p<0.01). (Figure 2) Conclusions: Using equation 1, CZE can be used to detect the presence of voxelotor and estimate its whole blood concentration. This will allow clinicians to have a better understanding of how their patients are using voxelotor. Additionally, higher calculated whole blood concentrations correlated with higher increases in Hb. It was previously shown that patients who receive higher doses of voxelotor have on average larger increases in Hb. If it could be shown that increasing concentration in an individual on voxelotor is associated with an increased Hb for that individual, then our method could also be used to help clinicians select and adjust doses of voxelotor in a similar manner to how HbF is used in hydroxyurea dosing. Figure 1 Figure 1. Disclosures Curtis: GBT: Consultancy. Minniti: CSL Behring: Other: Endpoint adjudicator; Bluebird Bio: Other: Endpoint adjudicator; F. Hoffmann-La Roche: Consultancy; Chiesi: Consultancy; Novo Nordisk: Consultancy; Forma: Consultancy; Novartis: Consultancy; GBT: Consultancy. Ngyuen Dang: GBT: Current Employment. Pochron: GBT: Current Employment. Campbell: GBT: Research Funding; Sebia: Research Funding.


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